Family_I.6

General

ESTHER family : Bacterial_lip_FamI.6

Comment :
This family corresponds to family I.6 of the classification of Arpigny and Jaeger (1999). These lipases differ from other bacterial lipases. They present high phospholipase A1 activity. The substrate-binding cavity contains two large hydrophobic acyl chain-binding pockets and a shallow and more polar third pocket that is capable of binding either a (short) fatty acid or a phospholipid head-group.

References (3)

Title : Structural basis of phospholipase activity of Staphylococcus hyicus lipase - Tiesinga_2007_J.Mol.Biol_371_447
Author(s) : Tiesinga JJ , van Pouderoyen G , Nardini M , Ransac S , Dijkstra BW
Ref : Journal of Molecular Biology , 371 :447 , 2007
Abstract : Tiesinga_2007_J.Mol.Biol_371_447
ESTHER : Tiesinga_2007_J.Mol.Biol_371_447
PubMedSearch : Tiesinga_2007_J.Mol.Biol_371_447
PubMedID: 17582438
Gene_locus related to this paper: stahy-lipas

Title : Lipases for biotechnology - Jaeger_2002_Curr.Opin.Biotechnol_13_390
Author(s) : Jaeger KE , Eggert T
Ref : Curr Opin Biotechnol , 13 :390 , 2002
Abstract : Jaeger_2002_Curr.Opin.Biotechnol_13_390
ESTHER : Jaeger_2002_Curr.Opin.Biotechnol_13_390
PubMedSearch : Jaeger_2002_Curr.Opin.Biotechnol_13_390
PubMedID: 12323363

Title : Bacterial lipolytic enzymes: classification and properties - Arpigny_1999_Biochem.J_343_177
Author(s) : Arpigny JL , Jaeger KE
Ref : Biochemical Journal , 343 :177 , 1999
Abstract : Arpigny_1999_Biochem.J_343_177
ESTHER : Arpigny_1999_Biochem.J_343_177
PubMedSearch : Arpigny_1999_Biochem.J_343_177
PubMedID: 10493927